PDBsum entry 1lua

Oxidoreductase

PDB id: 1lua

Contents

Protein chains

287 a.a. *

Ligands

NAP ×3

Waters ×712

* Residue conservation analysis

PDB id:

1lua

Name:

Oxidoreductase

Title:

Structure of methylene-tetrahydromethanopterin dehydrogenase from methylobacterium extorquens am1 complexed with NADP

Structure:

Methylene tetrahydromethanopterin dehydrogenase. Chain: a, b, c. Synonym: methylenetetrahydrofolate dehydrogenase. Engineered: yes

Source:

Methylobacterium extorquens. Organism_taxid: 272630. Strain: am1. Gene: mtda. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Trimer (from PQS)

Resolution:

1.90Å R-factor: 0.185 R-free: 0.222

Authors:

U.Ermler,C.H.Hagemeier,A.Roth,U.Demmer,W.Grabarse,E.Warkentin, J.A.Vorholt

Key ref:

U.Ermler et al. (2002). Structure of methylene-tetrahydromethanopterin dehydrogenase from methylobacterium extorquens AM1. Structure, 10, 1127-1137. PubMed id: 12176390 DOI: 10.1016/S0969-2126(02)00802-X

Date:

22-May-02 Release date: 11-Sep-02

Protein chains

P55818  (MTDA_METEA) -  Bifunctional protein MdtA from Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)

Seq: 288 a.a.

Struc: 287 a.a.

Enzyme reactions

• Enzyme class 1: E.C.1.5.1.- - ?????
• Enzyme class 2: E.C.1.5.1.5 - methylenetetrahydrofolate dehydrogenase (NADP(+)).

Pathway:

• Reaction: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP⁺ = (6R)-5,10- methenyltetrahydrofolate + NADPH

(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) (Bound ligand (Het Group name = NAP) corresponds exactly) = (6R)-5,10- methenyltetrahydrofolate + NADPH

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1016/S0969-2126(02)00802-X

Structure 10:1127-1137 (2002)

PubMed id: 12176390

Structure of methylene-tetrahydromethanopterin dehydrogenase from methylobacterium extorquens AM1.

U.Ermler, C.H.Hagemeier, A.Roth, U.Demmer, W.Grabarse, E.Warkentin, J.A.Vorholt.

ABSTRACT

NADP-dependent methylene-H(4)MPT dehydrogenase, MtdA, from Methylobacterium extorquens AM1 catalyzes the dehydrogenation of methylene-tetrahydromethanopterin and methylene-tetrahydrofolate with NADP(+) as cosubstrate. The X-ray structure of MtdA with and without NADP bound was established at 1.9 A resolution. The enzyme is present as a homotrimer. The alpha,beta fold of the monomer is related to that of methylene-H(4)F dehydrogenases, suggesting a common evolutionary origin. The position of the active site is located within a large crevice built up by the two domains of one subunit and one domain of a second subunit. Methylene-H(4)MPT could be modeled into the cleft, and crucial active site residues such as Phe18, Lys256, His260, and Thr102 were identified. The molecular basis of the different substrate specificities and different catalytic demands of MtdA compared to methylene-H(4)F dehydrogenases are discussed.

Selected figure(s)

Figure 1.
Figure 1. Reaction of MtdAMethylene-H[4]MPT (-H[4]F) is oxidized to methenyl-H[4]MPT (-H[4]F) with NADP+ as cosubstrate. H[4]MPT is composed of a 7-methyl-6-ethyl-pterin, an aminobenzyl, a 1-desoxyribose, a ribose, a phosphate, and a 2-hydroxyglutarate moiety. H[4]F consists of a 6-methyl-pterin, a p-aminobenzoate, and a glutamate moiety. The two methyl groups painted in blue are only present in H[4]MPT. Methylene and methenyl groups are indicated in red.

The above figure is reprinted by permission from Cell Press: Structure (2002, 10, 1127-1137) copyright 2002.

Figure was selected by an automated process.